ID G3GH25_STREE Unreviewed; 283 AA.
AC G3GH25;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rmlD {ECO:0000313|EMBL:AEO88826.1};
OS Streptococcus pneumoniae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313 {ECO:0000313|EMBL:AEO88826.1};
RN [1] {ECO:0000313|EMBL:AEO88826.1}
RP NUCLEOTIDE SEQUENCE.
RA Elberse K.E., Witteveen S., van der Heide H., van de Pol I., Schot C.,
RA van der Ende A., Berbers G., Schouls L.;
RT "Sequence Diversity within the Capsular Genes of Streptococcus pneumoniae
RT Serogroup 6 and 19.";
RL PLoS ONE 6:e25018-e25018(2011).
CC -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62830; EC=1.1.1.133;
CC Evidence={ECO:0000256|RuleBase:RU364082};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|RuleBase:RU364082}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
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DR EMBL; JF911524; AEO88826.1; -; Genomic_DNA.
DR AlphaFoldDB; G3GH25; -.
DR UniPathway; UPA00124; -.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR NCBIfam; TIGR01214; rmlD; 1.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT DOMAIN 2..280
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 283 AA; 32358 MW; 9D229DEB275A1916 CRC64;
MILITGANGQ LGTELRYLLD ERNEEYVAVD VAEMDITDAE MVEKVFEEVK PTLVYHCAAY
TAVDAAEDEG KELDFAINVT GTKNVARASE KHGATLVYIS TDYVFDGKKP VGQEWEVDDR
PDPQTEYGRT KRMGEELVEK HVSNFYIIRT AWVFGNYGKN FVFTMQNLAK THKTLTVVND
QYGRPTWTRT LAEFMTYLAE NRKEFGYYHL SNDATEDTTW YDFAVEILKD TDVEVKPVDS
SQFPAKAKRP LNSTMNLAKA KATGFVIPTW QDALQEFYKQ EVR
//
